WVSOM Class of 2012 Amino Acids and Protein Structure
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| at normal ph, amino groups have what charge? | positive
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| what are the hydrophobic amino acids? | glycine (G), alanine (A), proline (P), valine (V), leucine (L), isoleucine (I), phenylalanine (F), tyrosine (Y), tryptophan (W), methionine (M): (GAPVLIFYWM)
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| what are the branched chain amino acids? | valine (V), leucine (L), isoleucine (I)
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| which amino acids are non-polar and hydrophobic? | glycine (G), alanine (A), proline (P), valine (V), leucine (L), isoleucine (I), phenylalanine (F), methionine (M): (GAPVLIFM)
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| which amino acids are polar uncharged? | serine (S), threonine (T), tyrosine (Y), tryptophan (W), asparagine (N), glutamine (Q): (STYWNQ)
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| out of the polar uncharged amino acids, which have OH groups and can phosphorylate? | serine (S), threonine (T), tyrosine (Y): (STY)
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| the n-side chain is a common site for what? | glycosylation
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| what are the negatively charged amino acids? | aspartate (D), and glutamate (E): (D&E)
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| what is the backbone of an amino acid? | an alpha carbon + an amino group + a carboxyl group
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| aspartate and glutamate can form what bonds? | ionic and hydrogen bonds
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| what are the positively charged basic molecules? | arginine (R), lysine (K), and histidine (H)
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| how are arginine and lysine frequently modified? | acetylation and methylation
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| the pka of a histidine side chain is what? what does this help it to make? | 6.0; a good buffer
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| cystine is held by what kind of bonds? | disulfide
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| excess cystine can form what in humans? | calculi
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| phenylalanine is what structure? what does this cause it to do? | aromatic, it can stack
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| what amino acid causes kinks in the peptide chain? | proline
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| what are the 3 protein families? | globular, fibrous, and membrane-spanning
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| keratin is a classic example of what kind of bonds? | disulfide
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| rhodopsin has non-polar chains on the ____ and polar chains on the ____ | surface, interior
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| in hemoglobin, iron can be what forms? | Ferric (3+) or Ferrous (2+)
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| which heme can bind oxygen? | ferrous (2+)
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| heme group is a pocket of hydrophobic amino acids and what? | histidine residues
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| myoglobin is small and can therefore do what? | leak out of damaged cells
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| what is the primary hemoglobin in adults? | HbA
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| if the body wants to release oxygen, which form of hemoglobin will it use? if it wants to uptake oxygen? | taut, relaxed
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| when histidine is protonated, what happens to the oxygen in hemoglobin? | it gets released
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| 2,3-BPG forms when? | during glycolysis
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| what form of hemoglobin does 2,3-BPG stabilize? | taut form
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| methemoglobin binds to which Fe form? what must next happen | 3+, it must be reduced back ot 2+
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| decreased NADH methemoglobin reductase results in what condition? | methemoglobinemia (blue people of kentucky)
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| fetal hemoglobin binds more readily with what gas? | carbon monoxide
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| what letter represents leucine? | l
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| what letter represents phenylalanine? | f
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| what letter represents tyrosine? | y
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| what letter represents tryptopham? | w
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| what letter represents asparagine? | n
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| what letter represents glutamine? | q
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| what letter represents threonine? | t
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| what letter represents aspartate? | d
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| what letter represents glutamate? | e
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| what letter represents lysine? | k
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